Publikationsserver der Universitätsbibliothek Marburg
Titel:Das AUACCC-bindende Protein Khd4 kontrolliert Morphogenese und Pathogenität in Ustilago maydis
Autor:Vollmeister, Evelyn
Weitere Beteiligte: Feldbrügge, Michael (Prof.)
Veröffentlicht:2009
URI:https://archiv.ub.uni-marburg.de/diss/z2010/0125
URN: urn:nbn:de:hebis:04-z2010-01250
DOI: https://doi.org/10.17192/z2010.0125
DDC: Biowissenschaften, Biologie
Titel (trans.):The AUACCC-binding protein Khd4 regulates cell morphology and pathogenicity in Ustilago maydis
Publikationsdatum:2010-04-27
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
posttranskriptionelle Regulation, RNS-Bindungsproteine, Ustilago zeae, Hefe Drei-Hybrid System, K-Homologie Domäne, Ustilago, regulatorisches RNA-Element, Pathogenitaet, regulatory RNA element, yeast Three-Hybrid System, Microarray, Molekulare Bioinformatik, post-transcriptional regulation, K homology domain

Zusammenfassung:
Der phytopathogene Basidiomyzet Ustilago maydis ist der Erreger des Maisbeulenbrandes. Für eine erfolgreiche Infektion der Wirtspflanze Zea mays ist die Bildung eines dikaryotischen Filaments erforderlich. Erst in diesem Stadium kann der Pilz die Pflanzenoberfläche penetrieren und die Tumorbildung induzieren. U. maydis stellt nicht nur ein Modellsystem für die Pilz/Wirt-Interaktion dar, sondern wurde in der Vergangenheit bspw. auch für Untersuchungen der DNA-Reparatur oder der RNA-Biologie genutzt. Erste Charakterisierungen des Einflusses RNA-bindender Proteine auf die Pathogenität deuteten dabei an, dass die posttranskriptionelle Regulation innerhalb des infektiösen Stadiums eine bedeutende Rolle spielt. Jedoch wurden bisher nur wenige RNA-bindende Proteine hinsichtlich ihrer regulatorischen Funktion in filamentösen Pilzen näher charakterisiert. In dieser Arbeit wurde die Rolle des RNA-bindenden Proteins Khd4 von U. maydis detailliert untersucht. Die Deletion des Gens führt zu einem pleiotropen Phänotyp, der sich in einem Zytokinesedefekt haploider Sporidien, reduzierter Filamentbildung und stark verringerter Virulenz äußert. Um die Funktion von Khd4 hinsichtlich dessen Einfluss auf Morphologie und Pathogenität zu verstehen, wurde die RNA/Protein-Interaktion charakterisiert und mögliche Ziel-Transkripte identifiziert. In dieser Dissertation konnte gezeigt werden, dass die Tandem-KH-Domänen 3 und 4 essentiell für die Funktion von Khd4 und für die RNA-Bindung in vivo sind. Mutationen wichtiger Aminosäuren innerhalb dieser Domänen äußerten sich in einem dem khd4Δ-ähnlichen Phänotyp und verhinderten die Bindung AUACCC-enthaltender RNA, welches mit Hilfe des Hefe-Drei-Hybrid-Systems ermittelt werden konnte. Die Anwesenheit des cis-aktiven Elements AUACCC war dabei sowohl notwendig als auch hinreichend. Um zu untersuchen, ob es sich bei diesem Motiv um ein regulatorisches RNA-Element in U. maydis handelt, wurden zwei unabhängige Analysen durchgeführt. Zum einen wurde über Microarray-Analysen ermittelt, dass das Motiv AUACCC in differentiell regulierten mRNAs angereichert war (29 von 72 regulierten mRNAs). Über bioinformatische Analysen wurde zum anderen eine signifikante Anreicherung des Motivs in den ersten 150 Nukleotiden der 3untranslatierten Region (UTR) festgestellt. Die Untersuchung experimentell ermittelter 3UTR-Längen bestätigte dabei diese Anreicherung. Weiterhin war die überwiegende Mehrheit der differentiell regulierten Transkripte im khd4-Deletionsstamm hochreguliert, was für eine destabilisierende Funktion von Khd4 sprach. Unterstützt wurde diese Hypothese durch die partielle Kolokalisation von Khd4 mit processing bodies (prozessierenden Körpern, P-bodies), welche in mRNA-Abbauprozessen von hoher Bedeutung sind. Die 29 AUACCC-enthaltenden, differentiell deregulierten Transkripte stellen außerdem direkte Ziel-Transkripte dar, welche einen Einfluss auf den Phänotyp des khd4Δ-Stammes besitzen könnten. Folglich scheint die RNA-Bindung von Khd4 essentiell zu sein, um posttranskriptionell AUACCC-enthaltende mRNAs durch Rekrutierung von P-bodies zu degradieren. Mit Hilfe der Khd4-abhängigen Regulation wird dadurch möglicherweise die korrekte Entwicklung des haploiden und infektiösen Stadiums von U. maydis gewährleistet.

Bibliographie / References

  1. Becht, P. (2005) Die Rolle von RNA-bindenden Proteinen bei der pathogenen Entwicklung von Ustilago maydis. MPI for Terrestrial Microbiology. Philipps-University, Marburg.
  2. Bailey, T.L. und Elkan, C. (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc Int Conf Intell Syst Mol Biol, 2, 28-36.
  3. Valverde, R., Pozdnyakova, I., Kajander, T., Venkatraman, J. und Regan, L. (2007) Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein. Structure, 15, 1090- 1098.
  4. Gonsalvez, G.B., Urbinati, C.R. und Long, R.M. (2005) RNA localization in yeast: moving towards a mechanism. Biol Cell, 97, 75-86.
  5. Wilson, C.A., Kreychman, J. und Gerstein, M. (2000) Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores. J Mol Biol, 297, 233-249.
  6. Garcia-Mayoral, M.F., Hollingworth, D., Masino, L., Diaz-Moreno, I., Kelly, G., Gherzi, R., Chou, C.F., Chen, C.Y. und Ramos, A. (2007) The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation. Structure, 15, 485-498.
  7. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. und Lipman, D.J. (1990) Basic local alignment search tool. J Mol Biol, 215, 403-410.
  8. Kämper, J. (2004) A PCR-based system for highly efficient generation of gene replacement mutants in Ustilago maydis. Mol Genet Genomics, 271, 103-110.
  9. Brachmann, A., König, J., Julius, C. und Feldbrügge, M. (2004) A reverse genetic approach for generating gene replacement mutants in Ustilago maydis. Mol Genet Genomics, 272, 216-226.
  10. Gillissen, B., Bergemann, J., Sandmann, C., Schröer, B., Bölker, M. und Kahmann, R. (1992) A two-component regulatory system for self/non-self recognition in Ustilago maydis. Cell, 68, 647-657.
  11. Moore, M.J. und Proudfoot, N.J. (2009) Pre-mRNA processing reaches back to transcription and ahead to translation. Cell, 136, 688-700.
  12. Holliday, R. (2004) Early studies on recombination and DNA repair in Ustilago maydis. DNA Repair (Amst), 3, 671- 682.
  13. Doehlemann, G., Wahl, R., Vranes, M., de Vries, R.P., Kämper, J. und Kahmann, R. (2008) Establishment of compatibility in the Ustilago maydis/maize pathosystem. J Plant Physiol, 165, 29-40.
  14. Fierro-Monti, I. und Mathews, M.B. (2000) Proteins binding to duplexed RNA: one motif, multiple functions. Trends Biochem Sci, 25, 241-246.
  15. Kedersha, N. und Anderson, P. (2002) Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans, 30, 963-969.
  16. Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W. und Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res., 25, 3389-3402.
  17. Brykailo, M.A., Corbett, A.H. und Fridovich-Keil, J.L. (2007) Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160. Nucleic Acids Res, 35, 1108-1118.
  18. Bailey, T.L., Williams, N., Misleh, C. und Li, W.W. (2006) MEME: discovering and analyzing DNA and protein sequence motifs. Nucleic Acids Res, 34, W369-373.
  19. Letunic, I., Doerks, T. und Bork, P. (2009) SMART 6: recent updates and new developments. Nucleic Acids Res, 37, D229-232.
  20. Pascal, E. und Tjian, R. (1991) Different activation domains of Sp1 govern formation of multimers and mediate transcriptional synergism. Genes Dev, 5, 1646-1656.
  21. Crooks, G.E., Hon, G., Chandonia, J.M. und Brenner, S.E. (2004) WebLogo: a sequence logo generator. Genome Res, 14, 1188-1190.
  22. Weber, I., Gruber, C. und Steinberg, G. (2003) A class-V myosin required for mating, hyphal growth, and pathogenicity in the dimorphic plant pathogen Ustilago maydis. Plant Cell, 15, 2826-2842.
  23. Mahlert, M., Leveleki, L., Hlubek, A., Sandrock, B. und Bölker, M. (2006) Rac1 and Cdc42 regulate hyphal growth and cytokinesis in the dimorphic fungus Ustilago maydis. Mol Microbiol, 59, 567-578.
  24. Zarnack, K., Eichhorn, H., Kahmann, R. und Feldbrügge, M. (2008) Pheromone-regulated target genes respond differentially to MAPK phosphorylation of transcription factor Prf1. Mol Microbiol, 69, 1041-1053.
  25. Garcia-Muse, T., Steinberg, G. und Perez-Martin, J. (2004) Characterization of B-type cyclins in the smut fungus Ustilago maydis: roles in morphogenesis and pathogenicity. J Cell Sci, 117, 487-506.
  26. Böhmer, C., Böhmer, M., Bölker, M. und Sandrock, B. (2008) Cdc42 and the Ste20-like kinase Don3 act independently in triggering cytokinesis in Ustilago maydis. J Cell Sci, 121, 143-148.
  27. Reijns, M.A., Alexander, R.D., Spiller, M.P. und Beggs, J.D. (2008) A role for Q/N-rich aggregation-prone regions in P-body localization. J Cell Sci, 121, 2463-2472.
  28. Stumpf, C.R., Kimble, J. und Wickens, M. (2008) A Caenorhabditis elegans PUF protein family with distinct RNA binding specificity. Rna, 14, 1550-1557.
  29. Vanrobays, E., Leplus, A., Osheim, Y.N., Beyer, A.L., Wacheul, L. und Lafontaine, D.L. (2008) TOR regulates the subcellular distribution of DIM2, a KH domain protein required for cotranscriptional ribosome assembly and pre-40S ribosome export. Rna, 14, 2061-2073.
  30. König, J., Julius, C., Baumann, S., Homann, M., Göringer, H.U. und Feldbrügge, M. (2007) Combining SELEX and the yeast three-hybrid system for in vivo selection and classification of RNA aptamers. Rna, 13, 614-622.
  31. Teixeira, D., Sheth, U., Valencia-Sanchez, M.A., Brengues, M. und Parker, R. (2005) Processing bodies require RNA for assembly and contain nontranslating mRNAs. Rna, 11, 371-382.
  32. Schmidt, S., Bork, P. und Dandekar, T. (2002) A versatile structural domain analysis server using profile weight matrices. J Chem Inf Comput Sci, 42, 405-407.
  33. Brachmann, A. (2001) Die frühe Infektionsphase von Ustilago maydis: Genregulation durch das bW/bE-Heterodimer. Fakultät für Biologie. Ludwig-Maximilians-Universität, München.
  34. Gherzi, R., Trabucchi, M., Ponassi, M., Ruggiero, T., Corte, G., Moroni, C., Chen, C.Y., Khabar, K.S., Andersen, J.S. und Briata, P. (2006) The RNA-binding protein KSRP promotes decay of beta-catenin mRNA and is inactivated by PI3K-AKT signaling. PLoS Biol, 5, e5.
  35. Gherzi, R., Lee, K.Y., Briata, P., Wegmüller, D., Moroni, C., Karin, M. und Chen, C.Y. (2004) A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol Cell, 14, 571-583.
  36. Galgano, A., Forrer, M., Jaskiewicz, L., Kanitz, A., Zavolan, M. und Gerber, A.P. (2008) Comparative analysis of mRNA targets for human PUF-family proteins suggests extensive interaction with the miRNA regulatory system. PLoS ONE, 3, e3164.
  37. Marsellach, F.X., Huertas, D. und Azorin, F. (2006) The multi-KH domain protein of Saccharomyces cerevisiae Scp160p contributes to the regulation of telomeric silencing. J Biol Chem, 281, 18227-18235.
  38. Wahl, M.C., Will, C.L. und Lührmann, R. (2009) The spliceosome: design principles of a dynamic RNP machine. Cell, 136, 701-718.
  39. Böhmer, M., Colby, T., Böhmer, C., Bräutigam, A., Schmidt, J. und Bölker, M. (2007) Proteomic analysis of dimorphic transition in the phytopathogenic fungus Ustilago maydis. Proteomics, 7, 675-685.
  40. Musco, G., Stier, G., Joseph, C., Castiglione Morelli, M.A., Nilges, M., Gibson, T.J. und Pastore, A. (1996) Three- dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell, 85, 237-245.
  41. Zalfa, F., Achsel, T. und Bagni, C. (2006) mRNPs, polysomes or granules: FMRP in neuronal protein synthesis. Curr Opin Neurobiol, 16, 265-269.
  42. Steinberg, G., Wedlich-Söldner, R., Brill, M. und Schulz, I. (2001) Microtubules in the fungal pathogen Ustilago maydis are highly dynamic and determine cell polarity. J Cell Sci, 114, 609-622.
  43. Letunic, I., Copley, R.R., Schmidt, S., Ciccarelli, F.D., Doerks, T., Schultz, J., Ponting, C.P. und Bork, P. (2004) SMART 4.0: towards genomic data integration. Nucleic Acids Res, 32 Database issue, D142-144.
  44. Sambrook, J., Frisch, E.F. und Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. Cold Spring Harbour Laboratory Press, Cold Spring Harbour, New York.
  45. Hesketh, J. (2004) 3'-Untranslated regions are important in mRNA localization and translation: lessons from selenium and metallothionein. Biochem Soc Trans, 32, 990-993.
  46. Lutz, C.S. (2008) Alternative polyadenylation: a twist on mRNA 3' end formation. ACS Chem Biol, 3, 609-617.
  47. Mayorga, M.E. und Gold, S.E. (1999) A MAP kinase encoded by the ubc3 gene of Ustilago maydis is required for filamentous growth and full virulence. Mol. Microbiol., 34, 485-497.
  48. Grosset, C., Chen, C.Y., Xu, N., Sonenberg, N., Jacquemin-Sablon, H. und Shyu, A.B. (2000) A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell, 103, 29-40.
  49. Muralidharan, B., Bakthavachalu, B., Pathak, A. und Seshadri, V. (2007) A minimal element in 5'UTR of insulin mRNA mediates its translational regulation by glucose. FEBS Lett, 581, 4103-4108.
  50. Taylor, S.J. und Shalloway, D. (1994) An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature, 368, 867-871.
  51. Wickens, M., Bernstein, D.S., Kimble, J. und Parker, R. (2002) A PUF family portrait: 3'UTR regulation as a way of life. Trends Genet, 18, 150-157.
  52. Wedlich-Söldner, R., Bölker, M., Kahmann, R. und Steinberg, G. (2000) A putative endosomal t-SNARE links exo- and endocytosis in the phytopathogenic fungus Ustilago maydis. EMBO J, 19, 1974-1986.
  53. Hoffman, C.S. und Winston, F. (1987) A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of E. coli. Gene, 57, 267-272.
  54. Barreau, C., Paillard, L. und Osborne, H.B. (2005) AU-rich elements and associated factors: are there unifying principles? Nucleic Acids Res, 33, 7138-7150.
  55. Wilusz, C.J. und Wilusz, J. (2004) Bringing the role of mRNA decay in the control of gene expression into focus. Trends Genet, 20, 491-497.
  56. Banuett, F. und Herskowitz, I. (2002) Bud morphogenesis and the actin and microtubule cytoskeletons during budding in the corn smut fungus Ustilago maydis. Fungal Genet Biol, 37, 149-170.
  57. Mayorga, M.E. und Gold, S.E. (1998) Characterization and molecular genetic complementation of mutants affecting dimorphism in the fungus Ustilago maydis. Fungal Genet Biol, 24, 364-376.
  58. Ule, J., Jensen, K.B., Ruggiu, M., Mele, A., Ule, A. und Darnell, R.B. (2003) CLIP identifies Nova-regulated RNA networks in the brain. Science, 302, 1212-1215.
  59. McKnight, G.L., Reasoner, J., Gilbert, T., Sundquist, K.O., Hokland, B., McKernan, P.A., Champagne, J., Johnson, C.J., Bailey, M.C., Holly, R., O`Hara, P.J. und Oram, J.F. (1992) Cloning and expression of a cellular high density lipoprotein-binding protein that is up-regulated by cholesterol loading of cells. J Biol Chem, 267, 12131-12141.
  60. Burd, C.G. und Dreyfuss, G. (1994) Conserved structures and diversity of functions of RNA-binding proteins. Science, 265, 615-621.
  61. Ostareck-Lederer, A. und Ostareck, D.H. (2004) Control of mRNA translation and stability in haematopoietic cells: the function of hnRNPs K and E1/E2. Biol Cell, 96, 407-411.
  62. Aguilera, A. (2005) Cotranscriptional mRNP assembly: from the DNA to the nuclear pore. Curr Opin Cell Biol, 17, 242-250.
  63. Fenn, S., Du, Z., Lee, J.K., Tjhen, R., Stroud, R.M. und James, T.L. (2007) Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 A resolution. Nucleic Acids Res, 35, 2651-2660.
  64. Southern, E.M. (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol, 98, 503-517.
  65. Haag, C. (2008) Die funktionelle Charakterisierung des RNA-bindenden Proteins Khd4 in Ustilago maydis. MPI for Terrestrial Microbilogy. Philipps-Universität, Marburg.
  66. Bomsztyk, K., Van Seuningen, I., Suzuki, H., Denisenko, O. und Ostrowski, J. (1997) Diverse molecular interactions of the hnRNP K protein. FEBS Lett, 403, 113-115.
  67. Feng, Y., Absher, D., Eberhart, D.E., Brown, V., Malter, H.E. und Warren, S.T. (1997) FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol Cell, 1, 109-118.
  68. Vollmeister, E. (2005) Funktionelle und zellbiologische Untersuchungen an dem RNA-bindenden Protein Khd4 aus Ustilago maydis. MPI for Terrestrail Microbiology. Philipps-Universität, Marburg.
  69. Ho, E.C., Cahill, M.J. und Saville, B.J. (2007) Gene discovery and transcript analyses in the corn smut pathogen Ustilago maydis: expressed sequence tag and genome sequence comparison. BMC Genomics, 8, 334.
  70. Nicholas, K.B., Nicholas, H.B., Jr. und Deerfield, D.W., II. (1997) GeneDoc: Analysis and Visualization of Genetic Variation. EMBNEW.NEWS, 4.
  71. Bölker, M., Genin, S., Lehmler, C. und Kahmann, R. (1995) Genetic regulation of mating, and dimorphism in Ustilago maydis. Can J Bot, 73, 320-325.
  72. Huh, W.K., Falvo, J.V., Gerke, L.C., Carroll, A.S., Howson, R.W., Weissman, J.S. und O'Shea, E.K. (2003) Global analysis of protein localization in budding yeast. Nature, 425, 686-691.
  73. Spellig, T., Bottin, A. und Kahmann, R. (1996) Green fluorescent protein (GFP) as a new vital marker in the phytopathogenic fungus Ustilago maydis. Mol Gen Genet, 252, 503-509.
  74. Kim, H.H. und Gorospe, M. (2008) GU-rich RNA: expanding CUGBP1 function, broadening mRNA turnover. Mol Cell, 29, 151-152.
  75. Ostrowski, J., Wyrwicz, L., Rychlewski, L. und Bomsztyk, K. (2002) Heterogeneous nuclear ribonucleoprotein K protein associates with multiple mitochondrial transcripts within the organelle. J Biol Chem, 277, 6303-6310.
  76. Fukuda, T., Naiki, T., Saito, M. und Irie, K. (2009) hnRNP K interacts with RNA binding motif protein 42 and functions in the maintenance of cellular ATP level during stress conditions. Genes Cells, 14, 113-128.
  77. Bomsztyk, K., Denisenko, O. und Ostrowski, J. (2004) hnRNP K: one protein multiple processes. Bioessays, 26, 629- 638.
  78. Hui, J., Stangl, K., Lane, W.S. und Bindereif, A. (2003) HnRNP L stimulates splicing of the eNOS gene by binding to variable-length CA repeats. Nat Struct Biol, 10, 33-37.
  79. Dreyfuss, G., Matunis, M.J., Pinol-Roma, S. und Burd, C.G. (1993) hnRNP proteins and the biogenesis of mRNA. Annu Rev Biochem, 62, 289-321.
  80. Guerra, M., Dobbertin, A. und Legay, C. (2008) Identification of cis-acting elements involved in acetylcholinesterase RNA alternative splicing. Mol Cell Neurosci, 38, 1-14.
  81. Brachmann, A., Weinzierl, G., Kämper, J. und Kahmann, R. (2001) Identification of genes in the bW/bE regulatory cascade in Ustilago maydis. Mol Microbiol, 42, 1047-1063.
  82. Gish, W. und States, D.J. (1993) Identification of protein coding regions by database similarity search. Nat Genet, 3, 266-272.
  83. Holliday, R. (1961) Induced mitotic crossing-over in Ustilago maydis. Genet Res Camb, 2, 231-248.
  84. Tsukuda, T., Carleton, S., Fotheringham, S. und Holloman, W.K. (1988) Isolation and characterization of an autonomously replicating sequence from Ustilago maydis. Mol Cell Biol, 8, 3703-3709.
  85. Weinzierl, G. (2001) Isolierung und Charakterisierung von Komponenten der b-vermittelten Regulationskaskade in Ustilago maydis. Fachbereich Biologie. Philipps-Universität Marburg, Marburg.
  86. Currie, J.R. und Brown, W.T. (1999) KH domain-containing proteins of yeast: absence of a fragile X gene homologue. Am J Med Genet, 84, 272-276.
  87. Daigle, N. und Ellenberg, J. (2007) LambdaN-GFP: an RNA reporter system for live-cell imaging. Nat. Methods, 4, 633-636.
  88. Mikula, M., Dzwonek, A., Karczmarski, J., Rubel, T., Dadlez, M., Wyrwicz, L.S., Bomsztyk, K. und Ostrowski, J. (2006) Landscape of the hnRNP K protein-protein interactome. Proteomics, 6, 2395-2406.
  89. Kuersten, S. und Goodwin, E.B. (2005) Linking nuclear mRNP assembly and cytoplasmic destiny. Biol Cell, 97, 469- 478.
  90. Ostareck, D.H., Ostareck-Lederer, A., Shatsky, I.N. und Hentze, M.W. (2001) Lipoxygenase mRNA silencing in erythroid differentiation: The 3'UTR regulatory complex controls 60S ribosomal subunit joining. Cell, 104, 281-290.
  91. Paquin, N., Menade, M., Poirier, G., Donato, D., Drouet, E. und Chartrand, P. (2007) Local activation of yeast ASH1 mRNA translation through phosphorylation of Khd1p by the casein kinase Yck1p. Mol Cell, 26, 795- 809.
  92. Wilhelm, J.E. und Smibert, C.A. (2005) Mechanisms of translational regulation in Drosophila. Biol Cell, 97, 235-252.
  93. Dreyfuss, G., Kim, V.N. und Kataoka, N. (2002) Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol, 3, 195-205.
  94. Brengues, M., Teixeira, D. und Parker, R. (2005) Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science, 310, 486-489.
  95. Rougemaille, M., Villa, T., Gudipati, R.K. und Libri, D. (2008) mRNA journey to the cytoplasm: attire required. Biol Cell, 100, 327-342.
  96. Van de Bor, V. und Davis, I. (2004) mRNA localisation gets more complex. Curr Opin Cell Biol, 16, 300-307.
  97. Ostareck, D.H., Ostareck-Lederer, A., Wilm, M., Thiele, B.J., Mann, M. und Hentze, M.W. (1997) mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end. Cell, 89, 597-606.
  98. Zarnack, K. und Feldbrügge, M. (2007) mRNA trafficking in fungi. Mol Genet Genomics, 278, 347-359.
  99. Kämper, J., Reichmann, M., Romeis, T., Bölker, M. und Kahmann, R. (1995) Multiallelic recognition: nonself- dependent dimerization of the bE and bW homeodomain proteins in Ustilago maydis. Cell, 81, 73-83.
  100. White, S. und Doebley, J. (1998) Of genes and genomes and the origin of maize. Trends Genet, 14, 327-332.
  101. Parker, R. und Sheth, U. (2007) P bodies and the control of mRNA translation and degradation. Mol Cell, 25, 635- 646.
  102. Eulalio, A., Behm-Ansmant, I. und Izaurralde, E. (2007) P bodies: at the crossroads of post-transcriptional pathways. Nat Rev Mol Cell Biol, 8, 9-22.
  103. Innis, M.A., Gelfand, D.H., Sninsky, J.J. und White, T.J. (eds.). (1990) PCR Protocols: a guide to methods and applications. Academic Press, San Diego, USA.
  104. Diaz-Moreno, I., Hollingworth, D., Frenkiel, T.A., Kelly, G., Martin, S., Howell, S., Garcia-Mayoral, M., Gherzi, R., Briata, P. und Ramos, A. (2009) Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Nat Struct Mol Biol, 16, 238-246.
  105. Takizawa, P.A., DeRisi, J.L., Wilhelm, J.E. und Vale, R.D. (2000) Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science, 290, 341-344.
  106. Mangus, D.A., Evans, M.C. und Jacobson, A. (2003) Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol, 4, 223.
  107. Abdelmohsen, K., Kuwano, Y., Kim, H.H. und Gorospe, M. (2008) Posttranscriptional gene regulation by RNA- binding proteins during oxidative stress: implications for cellular senescence. Biol Chem, 389, 243-255.
  108. Vergara, S.V. und Thiele, D.J. (2008) Post-transcriptional regulation of gene expression in response to iron deficiency: co-ordinated metabolic reprogramming by yeast mRNA-binding proteins. Biochem Soc Trans, 36, 1088-1090.
  109. Blom, N., Sicheritz-Ponten, T., Gupta, R., Gammeltoft, S. und Brunak, S. (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics, 4, 1633-1649.
  110. Chen, Y. und Varani, G. (2005) Protein families and RNA recognition. Febs J, 272, 2088-2097.
  111. Koepke, J. (2005) Proteomvergleich zur Charakterisierung des RNA-bindenden Proteins Rrm4 in Ustilago maydis. MPI for Terrestrial Microbiology. Philipps-University, Marburg.
  112. Weber, V., Wernitznig, A., Hager, G., Harata, M., Frank, P. und Wintersberger, U. (1997) Purification and nucleic- acid-binding properties of a Saccharomyces cerevisiae protein involved in the control of ploidy. Eur J Biochem, 249, 309-317.
  113. Schmid, M. und Jensen, T.H. (2008) Quality control of mRNP in the nucleus. Chromosoma, 117, 419-429.
  114. Feldbrügge, M., Bölker, M., Steinberg, G., Kämper, J. und Kahmann, R. (2006) Regulatory and structural netwoks orchestrating mating, dimorphism, cell shape, and pathogenesis in Ustilago maydis. In Kües, U. und Fischer, R. (eds.), The Mycota I. Springer-Verlag, Berlin Heidelberg, pp. 375-391.
  115. Lee, M.H. und Schedl, T. (2006) RNA-binding proteins. WormBook, 1-13.
  116. Lunde, B.M., Moore, C. und Varani, G. (2007) RNA-binding proteins: modular design for efficient function. Nat Rev Mol Cell Biol, 8, 479-490.
  117. Anderson, P. und Kedersha, N. (2006) RNA granules. J Cell Biol, 172, 803-808.
  118. Bolognani, F. und Perrone-Bizzozero, N.I. (2008) RNA-protein interactions and control of mRNA stability in neurons. J Neurosci Res, 86, 481-489.
  119. Clery, A., Blatter, M. und Allain, F.H. (2008) RNA recognition motifs: boring? Not quite. Curr Opin Struct Biol, 18, 290-298.
  120. Keene, J.D. (2007) RNA regulons: coordination of post-transcriptional events. Nat Rev Genet, 8, 533-543.
  121. Cote, J., Boisvert, F.M., Boulanger, M.C., Bedford, M.T. und Richard, S. (2003) Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. Mol Biol Cell, 14, 274-287.
  122. Lukong, K.E. und Richard, S. (2003) Sam68, the KH domain-containing superSTAR. Biochim Biophys Acta, 1653, 73- 86.
  123. Li, A.M., Watson, A. und Fridovich-Keil, J.L. (2003) Scp160p associates with specific mRNAs in yeast. Nucleic Acids Res, 31, 1830-1837.
  124. Lewis, H.A., Musunuru, K., Jensen, K.B., Edo, C., Chen, H., Darnell, R.B. und Burley, S.K. (2000) Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome. Cell, 100, 323-332.
  125. Carbo, N. und Perez-Martin, J. (2008) Spa2 is required for morphogenesis but it is dispensable for pathogenicity in the phytopathogenic fungus Ustilago maydis. Fungal Genet Biol, 45, 1315-1327.
  126. Brown, J.W., Simpson, C.G., Thow, G., Clark, G.P., Jennings, S.N., Medina-Escobar, N., Haupt, S., Chapman, S.C. und Oparka, K.J. (2002) Splicing signals and factors in plant intron removal. Biochem Soc Trans, 30, 146-149.
  127. Hoyle, N.P., Castelli, L.M., Campbell, S.G., Holmes, L.E. und Ashe, M.P. (2007) Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P- bodies. J Cell Biol, 179, 65-74.
  128. Anderson, P. und Kedersha, N. (2008) Stress granules: the Tao of RNA triage. Trends Biochem Sci, 33, 141-150.
  129. Messias, A.C. und Sattler, M. (2004) Structural basis of single-stranded RNA recognition. Acc Chem Res, 37, 279-287.
  130. Braddock, D.T., Louis, J.M., Baber, J.L., Levens, D. und Clore, G.M. (2002b) Structure and dynamics of KH domains from FBP bound to single-stranded DNA. Nature, 415, 1051-1056.
  131. Valverde, R., Edwards, L. und Regan, L. (2008) Structure and function of KH domains. Febs J, 275, 2712-2726.
  132. Triezenberg, S.J. (1995) Structure and function of transcriptional activation domains. Curr Opin Genet Dev, 5, 190-196.
  133. D'Angelo, M.A. und Hetzer, M.W. (2008) Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol, 18, 456-466.
  134. Banerjee, P., Nayar, S., Hebbar, S., Fox, C.F., Jacobs, M.C., Park, J.H., Fernandes, J.J. und Dockendorff, T.C. (2007) Substitution of critical isoleucines in the KH domains of Drosophila fragile X protein results in partial loss- of-function phenotypes. Genetics, 175, 1241-1250.
  135. Lukong, K.E. und Richard, S. (2007) Targeting the RNA-binding protein Sam68 as a treatment for cancer? Future Oncol, 3, 539-544.
  136. Übersax, J.A., Woodbury, E.L., Quang, P.N., Paraz, M., Blethrow, J.D., Shah, K., Shokat, K.M. und Morgan, D.O. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature, 425, 859-864.
  137. Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. und Higgins, D.G. (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res, 25, 4876-4882.
  138. Parker, R. und Song, H. (2004) The enzymes and control of eukaryotic mRNA turnover. Nat Struct Mol Biol, 11, 121- 127.
  139. Gibson, T.J., Thompson, J.D. und Heringa, J. (1993) The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid. FEBS Lett, 324, 361-366.
  140. Van Seuningen, I., Ostrowski, J., Bustelo, X.R., Sleath, P.R. und Bomsztyk, K. (1995) The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3- binding sites. Implications that K protein acts as a docking platform. J Biol Chem, 270, 26976-26985.
  141. Müller, P., Aichinger, C., Feldbrügge, M. und Kahmann, R. (1999) The MAP kinase kpp2 regulates mating and pathogenic development in Ustilago maydis. Mol Microbiol, 34, 1007-1017.
  142. Nechama, M., Ben-Dov, I.Z., Briata, P., Gherzi, R. und Naveh-Many, T. (2008) The mRNA decay promoting factor K-homology splicing regulator protein post-transcriptionally determines parathyroid hormone mRNA levels. Faseb J, 22, 3458-3468.
  143. Buckanovich, R.J., Yang, Y.Y. und Darnell, R.B. (1996) The onconeural antigen Nova-1 is a neuron-specific RNA- binding protein, the activity of which is inhibited by paraneoplastic antibodies. J Neurosci, 16, 1114-1122.
  144. Kuersten, S. und Goodwin, E.B. (2003) The power of the 3' UTR: translational control and development. Nat Rev Genet, 4, 626-637.
  145. Hornik, K. (2009) The R FAQ. [WWW document]: URL http://CRAN.R-project.org/doc/FAQ/R-FAQ.html.
  146. Becht, P., König, J. und Feldbrügge, M. (2006) The RNA-binding protein Rrm4 is essential for polarity in Ustilago maydis and shuttles along microtubules. J Cell Sci, 119, 4964-4973.
  147. Steinberg, G. und Fuchs, U. (2004) The role of microtubules in cellular organization and endocytosis in the plant pathogen Ustilago maydis. J Microsc, 214, 114-123.
  148. Banks, G.R., Shelton, P.A., Kanuga, N., Holden, D.W. und Spanos, A. (1993) The Ustilago maydis nar1 gene encoding nitrate reductase activity: sequence and transcriptional regulation. Gene, 131, 69-78.
  149. Andrews, D.L., Egan, J.D., Mayorga, M.E. und Gold, S.E. (2000) The Ustilago maydis ubc4 and ubc5 genes encode members of a MAP kinase cascade required for filamentous growth. Mol Plant Microbe Interact, 13, 781-786.
  150. Guo, M., Aston, C., Burchett, S.A., Dyke, C., Fields, S., Rajarao, S.J., Uetz, P., Wang, Y., Young, K. und Dohlman, H.G. (2003) The yeast G protein alpha subunit Gpa1 transmits a signal through an RNA binding effector protein Scp160. Mol Cell, 12, 517-524.
  151. Gerber, H.P., Seipel, K., Georgiev, O., Hofferer, M., Hug, M., Rusconi, S. und Schaffner, W. (1994) Transcriptional activation modulated by homopolymeric glutamine and proline stretches. Science, 263, 808-811.
  152. Radford, H.E., Meijer, H.A. und de Moor, C.H. (2008) Translational control by cytoplasmic polyadenylation in Xenopus oocytes. Biochim Biophys Acta, 1779, 217-229.
  153. Farina, K.L., Hüttelmaier, S., Musunuru, K., Darnell, R. und Singer, R.H. (2003) Two ZBP1 KH domains facilitate beta-actin mRNA localization, granule formation, and cytoskeletal attachment. J Cell Biol, 160, 77-87.
  154. Mignone, F., Gissi, C., Liuni, S. und Pesole, G. (2002) Untranslated regions of mRNAs. Genome Biol, 3, REVIEWS0004.
  155. Bölker, M. (2001) Ustilago maydis -a valuable model system for the study of fungal dimorphism and virulence. Microbiology, 147, 1395-1401.
  156. König, J. (2003) Verwendung des Drei-Hybrid-Systems zur Identifizierung eines RNA-Interaktionspartners von Rrm4 aus Ustilago maydis. MPI for Terrestrial Microbiology, Marburg. Ludwig-Maximilians-Universität, München.
  157. Margeot, A., Garcia, M., Wang, W., Tetaud, E., di Rago, J.P. und Jacq, C. (2005) Why are many mRNAs translated to the vicinity of mitochondria: a role in protein complex assembly? Gene, 354, 64-71.
  158. Backe, P.H., Messias, A.C., Ravelli, R.B., Sattler, M. und Cusack, S. (2005) X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids. Structure, 13, 1055- 1067.
  159. Wintersberger, U., Kühne, C. und Karwan, A. (1995) Scp160p, a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum, is necessary for maintenance of exact ploidy. Yeast, 11, 929-944.
  160. Blom, N., Gammeltoft, S. und Brunak, S. (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol, 294, 1351-1362.
  161. Messias, A.C., Harnisch, C., Ostareck-Lederer, A., Sattler, M. und Ostareck, D.H. (2006) The DICE-binding activity of KH domain 3 of hnRNP K is affected by c-Src-mediated tyrosine phosphorylation. J Mol Biol, 361, 470- 481.
  162. Müller, M., Heuck, A. und Niessing, D. (2007) Directional mRNA transport in eukaryotes: lessons from yeast. Cell Mol Life Sci, 64, 171-180.
  163. Feldbrügge, M., Zarnack, K., Vollmeister, E., Baumann, S., Koepke, J., König, J., Münsterkötter, M. und Mannhaupt, G. (2008) The posttranscriptional machinery of Ustilago maydis. Fungal Genet Biol, 45 Suppl 1, S40-46.
  164. Zhang, N., Ismail, T., Wu, J., Woodwark, K.C., Gardner, D.C., Walmsley, R.M. und Oliver, S.G. (1999) Disruption of six novel ORFs on the left arm of chromosome XII reveals one gene essential for vegetative growth of Saccharomyces cerevisiae. Yeast, 15, 1287-1296.
  165. Holliday, R. (1974) Ustilago maydis. In King, R.C. (ed.), Handbook of Genetics. Plenum Press, New York, USA, Vol. 1, pp. 575-595.
  166. Zakharkin, S.O., Kim, K., Mehta, T., Chen, L., Barnes, S., Scheirer, K.E., Parrish, R.S., Allison, D.B. und Page, G.P. (2005) Sources of variation in Affymetrix microarray experiments. BMC Bioinformatics, 6, 214.
  167. Noe, G., De Gaudenzi, J.G. und Frasch, A.C. (2008) Functionally related transcripts have common RNA motifs for specific RNA-binding proteins in trypanosomes. BMC Mol Biol, 9, 107.
  168. Frey, S., Pool, M. und Seedorf, M. (2001) Scp160p, an RNA-binding, polysome-associated protein, localizes to the endoplasmic reticulum of Saccharomyces cerevisiae in a microtubule-dependent manner. J Biol Chem, 276, 15905-15912.
  169. Pool, M.R. (2005) Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review). Mol Membr Biol, 22, 3-15.
  170. Lang, B.D. und Fridovich-Keil, J.L. (2000) Scp160p, a multiple KH-domain protein, is a component of mRNP complexes in yeast. Nucleic Acids Res, 28, 1576-1584.
  171. Olivier, C., Poirier, G., Gendron, P., Boisgontier, A., Major, F. und Chartrand, P. (2005) Identification of a conserved RNA motif essential for She2p recognition and mRNA localization to the yeast bud. Mol Cell Biol, 25, 4752-4766.
  172. Hui, J., Hung, L.H., Heiner, M., Schreiner, S., Neumüller, N., Reither, G., Haas, S.A. und Bindereif, A. (2005) Intronic CA-repeat and CA-rich elements: a new class of regulators of mammalian alternative splicing. Embo J, 24, 1988-1998.
  173. Kruse, C., Grünweller, A., Notbohm, H., Kugler, S., Purschke, W.G. und Müller, P.K. (1996) Evidence for a novel cytoplasmic tRNA-protein complex containing the KH-multidomain protein vigilin. Biochem J, 320 Pt 1, 247-252.
  174. Kruse, C., Grünweller, A., Willkomm, D.K., Pfeiffer, T., Hartmann, R.K. und Müller, P.K. (1998) tRNA is entrapped in similar, but distinct, nuclear and cytoplasmic ribonucleoprotein complexes, both of which contain vigilin and elongation factor 1 alpha. Biochem J, 329 Pt 3, 615-621.
  175. Kruse, C., Willkomm, D.K., Grünweller, A., Vollbrandt, T., Sommer, S., Busch, S., Pfeiffer, T., Brinkmann, J., Hartmann, R.K. und Müller, P.K. (2000) Export and transport of tRNA are coupled to a multi-protein complex. Biochem J, 346 Pt 1, 107-115.
  176. Baum, S., Bittins, M., Frey, S. und Seedorf, M. (2004) Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes. Biochem J, 380, 823-830.
  177. Irie, K., Tadauchi, T., Takizawa, P.A., Vale, R.D., Matsumoto, K. und Herskowitz, I. (2002) The Khd1 protein, which has three KH RNA-binding motifs, is required for proper localization of ASH1 mRNA in yeast. Embo J, 21, 1158-1167.
  178. Braddock, D.T., Baber, J.L., Levens, D. und Clore, G.M. (2002a) Molecular basis of sequence-specific single- stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA. Embo J, 21, 3476-3485.
  179. Sengupta, D.J., Wickens, M. und Fields, S. (1999) Identification of RNAs that bind to a specific protein using the yeast three-hybrid system. Rna, 5, 596-601.
  180. McLaren, M., Asai, K. und Cochrane, A. (2004) A novel function for Sam68: enhancement of HIV-1 RNA 3' end processing. Rna, 10, 1119-1129.
  181. Hook, B., Bernstein, D., Zhang, B. und Wickens, M. (2005) RNA-protein interactions in the yeast three-hybrid system: affinity, sensitivity, and enhanced library screening. Rna, 11, 227-233.
  182. Deutschbauer, A.M., Williams, R.M., Chu, A.M. und Davis, R.W. (2002) Parallel phenotypic analysis of sporulation and postgermination growth in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A, 99, 15530-15535.
  183. van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E. und Seraphin, B. (2002) Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. Embo J, 21, 6915-6924.
  184. Ström, A.C., Forsberg, M., Lillhager, P. und Westin, G. (1996) The transcription factors Sp1 and Oct-1 interact physically to regulate human U2 snRNA gene expression. Nucleic Acids Res, 24, 1981-1986.
  185. Fleischer, T.C., Weaver, C.M., McAfee, K.J., Jennings, J.L. und Link, A.J. (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev, 20, 1294-1307.
  186. Colot, H.V., Park, G., Turner, G.E., Ringelberg, C., Crew, C.M., Litvinkova, L., Weiss, R.L., Borkovich, K.A. und Dunlap, J.C. (2006) A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors. Proc Natl Acad Sci U S A, 103, 10352-10357.
  187. Seay, D., Hook, B., Evans, K. und Wickens, M. (2006) A three-hybrid screen identifies mRNAs controlled by a regulatory protein. Rna, 12, 1594-1600.
  188. Fuchs, U., Hause, G., Schuchardt, I. und Steinberg, G. (2006) Endocytosis is essential for pathogenic development in the corn smut fungus Ustilago maydis. Plant Cell, 18, 2066-2081.
  189. Scherer, M., Heimel, K., Starke, V. und Kämper, J. (2006) The Clp1 protein is required for clamp formation and pathogenic development of Ustilago maydis. Plant Cell, 18, 2388-2401.
  190. Garcia, M., Darzacq, X., Delaveau, T., Jourdren, L., Singer, R.H. und Jacq, C. (2007) Mitochondria-associated yeast mRNAs and the biogenesis of molecular complexes. Mol Biol Cell, 18, 362-368.
  191. Cunningham, K.S., Dodson, R.E., Nagel, M.A., Shapiro, D.J. und Schoenberg, D.R. (2000) Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3'-untranslated region by the mRNA endonuclease polysomal ribonuclease 1. Proc Natl Acad Sci U S A, 97, 12498-12502.
  192. Brengues, M. und Parker, R. (2007) Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P- bodies in Saccharomyces cerevisiae. Mol Biol Cell, 18, 2592-2602.
  193. Stöhr, N., Lederer, M., Reinke, C., Meyer, S., Hatzfeld, M., Singer, R.H. und Hüttelmaier, S. (2006) ZBP1 regulates mRNA stability during cellular stress. J Cell Biol, 175, 527-534.
  194. Shepard, K.A., Gerber, A.P., Jambhekar, A., Takizawa, P.A., Brown, P.O., Herschlag, D., DeRisi, J.L. und Vale, R.D. (2003) Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-localized transcripts using DNA microarray analysis. Proc Natl Acad Sci U S A, 100, 11429-11434.
  195. Kislauskis, E.H., Li, Z., Singer, R.H. und Taneja, K.L. (1993) Isoform-specific 3'-untranslated sequences sort alpha- cardiac and beta-cytoplasmic actin messenger RNAs to different cytoplasmic compartments. J Cell Biol, 123, 165-172.
  196. Bashkirov, V.I., Scherthan, H., Solinger, J.A., Buerstedde, J.M. und Heyer, W.D. (1997) A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J Cell Biol, 136, 761-773.
  197. Kedersha, N., Stoecklin, G., Ayodele, M., Yacono, P., Lykke-Andersen, J., Fitzler, M.J., Scheuner, D., Kaufman, R.J., Golan, D.E. und Anderson, P. (2005) Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol, 169, 871-884.
  198. Cougot, N., Babajko, S. und Seraphin, B. (2004) Cytoplasmic foci are sites of mRNA decay in human cells. J Cell Biol, 165, 31-40.
  199. Wang, H., Dictenberg, J.B., Ku, L., Li, W., Bassell, G.J. und Feng, Y. (2008) Dynamic association of the fragile X mental retardation protein as a messenger ribonucleoprotein between microtubules and polyribosomes. Mol Biol Cell, 19, 105-114.
  200. Mendelsohn, B.A., Li, A.M., Vargas, C.A., Riehman, K., Watson, A. und Fridovich-Keil, J.L. (2003) Genetic and biochemical interactions between SCP160 and EAP1 in yeast. Nucleic Acids Res, 31, 5838-5847.
  201. Abaza, I. und Gebauer, F. (2008) Functional domains of Drosophila UNR in translational control. Rna, 14, 482-490.
  202. Ross, A.F., Oleynikov, Y., Kislauskis, E.H., Taneja, K.L. und Singer, R.H. (1997) Characterization of a beta-actin mRNA zipcode-binding protein. Mol Cell Biol, 17, 2158-2165.
  203. Vlasova, I.A., Tahoe, N.M., Fan, D., Larsson, O., Rattenbacher, B., Sternjohn, J.R., Vasdewani, J., Karypis, G., Reilly, C.S., Bitterman, P.B. und Bohjanen, P.R. (2008) Conserved GU-rich elements mediate mRNA decay by binding to CUG-binding protein 1. Mol Cell, 29, 263-270.
  204. Hogan, D.J., Riordan, D.P., Gerber, A.P., Herschlag, D. und Brown, P.O. (2008) Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system. PLoS Biol, 6, e255.
  205. Hasegawa, Y., Irie, K. und Gerber, A.P. (2008) Distinct roles for Khd1p in the localization and expression of bud- localized mRNAs in yeast. Rna, 14, 2333-2347.
  206. Merritt, C., Rasoloson, D., Ko, D. und Seydoux, G. (2008) 3' UTRs are the primary regulators of gene expression in the C. elegans germline. Curr Biol, 18, 1476-1482.
  207. Licatalosi, D.D., Mele, A., Fak, J.J., Ule, J., Kayikci, M., Chi, S.W., Clark, T.A., Schweitzer, A.C., Blume, J.E., Wang, X., Darnell, J.C. und Darnell, R.B. (2008) HITS-CLIP yields genome-wide insights into brain alternative RNA processing. Nature, 456, 464-469.
  208. König, J., Baumann, S., Koepke, J., Pohlmann, T., Zarnack, K. und Feldbrügge, M. (2009) The fungal RNA-binding protein Rrm4 mediates long-distance transport of ubi1 and rho3 mRNAs. Embo J.
  209. Kaffarnik, F., Müller, P., Leibundgut, M., Kahmann, R. und Feldbrügge, M. (2003) PKA and MAPK phosphorylation of Prf1 allows promoter discrimination in Ustilago maydis. EMBO J, 22, 5817-5826.
  210. Martin, K.C. und Ephrussi, A. (2009) mRNA localization: gene expression in the spatial dimension. Cell, 136, 719- 730.
  211. Banuett, F. und Herskowitz, I. (1989) Different a alleles of Ustilago maydis are necessary for maintenance of filamentous growth but not for meiosis. Proc Natl Acad Sci USA, 86, 5878-5882.
  212. Grishin, N.V. (2001) KH domain: one motif, two folds. Nucleic Acids Res, 29, 638-643.
  213. Siomi, H., Matunis, M.J., Michael, W.M. und Dreyfuss, G. (1993) The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res, 21, 1193-1198.
  214. Vasudevan, S. und Steitz, J.A. (2007) AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2. Cell, 128, 1105-1118.
  215. Schultz, J., Milpetz, F., Bork, P. und Ponting, C.P. (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci U S A, 95, 5857-5864.
  216. Emili, A., Greenblatt, J. und Ingles, C.J. (1994) Species-specific interaction of the glutamine-rich activation domains of Sp1 with the TATA box-binding protein. Mol Cell Biol, 14, 1582-1593.
  217. Weng, Z., Thomas, S.M., Rickles, R.J., Taylor, J.A., Brauer, A.W., Seidel-Dugan, C., Michael, W.M., Dreyfuss, G. und Brugge, J.S. (1994) Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains. Mol Cell Biol, 14, 4509-4521.
  218. Bassell, G.J. und Warren, S.T. (2008) Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function. Neuron, 60, 201-214.
  219. SenGupta, D.J., Zhang, B., Kraemer, B., Pochart, P., Fields, S. und Wickens, M. (1996) A three-hybrid system to detect RNA-protein interactions in vivo. Proc Natl Acad Sci U S A, 93, 8496-8501.
  220. Spellig, T., Bölker, M., Lottspeich, F., Frank, R.W. und Kahmann, R. (1994) Pheromones trigger filamentous growth in Ustilago maydis. EMBO J, 13, 1620-1627.
  221. Cohen, S.N., Chang, A.C. und Hsu, L. (1972) Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci U S A, 69, 2110-2114.
  222. Musunuru, K. und Darnell, R.B. (2004) Determination and augmentation of RNA sequence specificity of the Nova K-homology domains. Nucleic Acids Res, 32, 4852-4861.
  223. Li, A.M., Vargas, C.A., Brykailo, M.A., Openo, K.K., Corbett, A.H. und Fridovich-Keil, J.L. (2004) Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast. Nucleic Acids Res, 32, 4768-4775.
  224. Gilks, N., Kedersha, N., Ayodele, M., Shen, L., Stoecklin, G., Dember, L.M. und Anderson, P. (2004) Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell, 15, 5383-5398.
  225. Becht, P., Vollmeister, E. und Feldbrügge, M. (2005) Role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis. Eukaryot Cell, 4, 121-133.
  226. Li, C. und Hung Wong, W. (2001) Model-based analysis of oligonucleotide arrays: model validation, design issues and standard error application. Genome Biol, 2, RESEARCH0032.
  227. Lang, B.D., Li, A., Black-Brewster, H.D. und Fridovich-Keil, J.L. (2001) The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast. Nucleic Acids Res, 29, 2567-2574.
  228. Schulz, B., Banuett, F., Dahl, M., Schlesinger, R., Schäfer, W., Martin, T., Herskowitz, I. und Kahmann, R. (1990) The b alleles of U. maydis, whose combinations program pathogenic development, code for polypeptides containing a homeodomain-related motif. Cell, 60, 295-306.

* Das Dokument ist im Internet frei zugänglich - Hinweise zu den Nutzungsrechten
© UB Marburg 1997 - 2024 Universitätsbibliothek Marburg